Calcyclin-Like Protein from Ehrlich Ascites Tumour Cells - Ca2+ -Binding Properties, Distribution and Target Protein

  • Jacek Kuznicki
  • Anna Filipek
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)


We have purified to homogeneity a 10.5 kDa Ca2+-binding protein from Ehrlich ascites tumour (EAT) cells (Kuznicki & Filipek, 1987). This protein differs from S-100 protein, calbindin 9k, parvalbumin and on comodulin by several criteria such as electrophoretic mobility in SDS- or urea-polyacrylamide gels, amino acid composition, and lack of cross-reactivity with the antibodies specific to these Ca2+-binding proteins. Recently, we found that the partial amino acid sequence of the 10.5 kDa Ca2+- binding protein from EAT cells is homologous to that of human calcyclin, and therefore we call the mouse protein a calcydin-like protein (Kuznicki et al., 1989a). Calcyclin is the name given to the growth factor-inducible gene (Calabretta et al., 1986a; 1986b). It has been suggested that calcyclin protein is involved in the control of cell proliferation and may bind Ca2+, as deduced from nucleotide sequence of the gene. To our best knowledge nobody has so far studied the protein itself.


Calcium Binding Protein Ehrlich Ascites Tumour Cell Ehrlich Ascites Tumour Partial Amino Acid Sequence Normal Mouse Tissue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Calabretta, B., Venturelli, D., Kaczmarek, L., Narni, F., Talpaz, M., Anderson, B., Beran M., and Baserga R., 1986, Altered expression of G.-specific genes in human malignant myeloid cells, Proc. Natl. Acad. Sci. U.S A., 83:1495.PubMedCrossRefGoogle Scholar
  2. Calabretta, B., Battini, R., Kaczmarek, L., de Riel, J. K., and Baserga, R., 1986, Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein, J. Biol. Chem, 261:12628.PubMedGoogle Scholar
  3. Filipek, A., Heizmann, C. W., and Kunicki, J., Zinc binding and dimer formation by calcyclin-like calcium binding protein from Ehrlich ascites tumour cells, in: “Proceedings of First European Symposium on Calcium Binding Proteins in Normal and Transformed Cells”, R. Pochet, D.E.M. Lawson and C.W. Heizmann, eds., Plenum Press (1989)Google Scholar
  4. Glenney J. R. Jr., Boudreau M., Galyean R., Hunter T., and Tack B., 1986, Association of the S-100-related Calpactin I light chain with NH2-terminal tail of the 36-kDa heavy chain. J. Biol. Chem., 261:10485.PubMedGoogle Scholar
  5. Kligman D., and Hilt, D.C., 1988, The S-100 protein family. Trends in Biochem. Sci., 13: 437.CrossRefGoogle Scholar
  6. Kunicki, J., and Filipek, A., 1987, Purification and properties of a novel Ca2+-binding protein (10.5 kDa) from Ehrlich-ascites-tumour cells. Biochem. J., 247: 663.Google Scholar
  7. Kunicki, J., Filipek, A., Hunziker, P. E., Huber, S., and Heizmann, C. W., 1989a, Calcium binding protein from mouse Ehrlich ascites tumour cells is homologous to human calcyclin. Biochem. J., in press.Google Scholar
  8. Kunicki, J., Filipek, A., Heimann, P., Kaczmarek, L., Kaminska, B., 1989b, Tissue specific distribution of the calcyclin-like 10.5 kDa calcium binding protein. FEBS Lett., in press.Google Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Jacek Kuznicki
    • 1
  • Anna Filipek
    • 1
  1. 1.Nencki Institute of Experimental BiologyWarsawPoland

Personalised recommendations